HHsearch alignment for GI: 254781074 and conserved domain: TIGR00628

>TIGR00628 ung uracil-DNA glycosylase; InterPro: IPR002043 Uracil-DNA glycosylase 3.2.2 from EC (UNG) is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses . In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human UNG1 protein is transported to both the mitochondria and the nucleus . The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation , but the presence of a mitochondrial transit peptide has not been directly demonstrated. The most N-terminal conserved region contains an aspartic acid residue which has been proposed, based on X-ray structures , to act as a general base in the catalytic mechanism. ; GO: 0004844 uracil DNA N-glycosylase activity, 0006284 base-excision repair.